8B1P

Crystal structure of SUDV VP40 CCS mutant

8B1P の概要

• エントリーDOI: 10.2210/pdb8b1p/pdb
• 分子名称: Matrix protein VP40 (2 entities in total)
• 機能のキーワード: ebola virus, sudv, vp40, matrix protein, dimer, viral protein
• 由来する生物種: Sudan ebolavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32571.49

構造登録者

Werner, A.-D.,Becker, S. (登録日: 2022-09-11, 公開日: 2023-06-21, 最終更新日: 2024-02-07)

主引用文献

Werner, A.D.,Schauflinger, M.,Norris, M.J.,Kluver, M.,Trodler, A.,Herwig, A.,Brandstadter, C.,Dillenberger, M.,Klebe, G.,Heine, A.,Saphire, E.O.,Becker, K.,Becker, S.
The C-terminus of Sudan ebolavirus VP40 contains a functionally important CX n C motif, a target for redox modifications.
Structure, 31:1038-, 2023

PubMed Abstract: The Ebola virus matrix protein VP40 mediates viral budding and negatively regulates viral RNA synthesis. The mechanisms by which these two functions are exerted and regulated are unknown. Using a high-resolution crystal structure of Sudan ebolavirus (SUDV) VP40, we show here that two cysteines in the flexible C-terminal arm of VP40 form a stabilizing disulfide bridge. Notably, the two cysteines are targets of posttranslational redox modifications and interact directly with the host`s thioredoxin system. Mutation of the cysteines impaired the budding function of VP40 and relaxed its inhibitory role for viral RNA synthesis. In line with these results, the growth of recombinant Ebola viruses carrying cysteine mutations was impaired and the released viral particles were elongated. Our results revealed the exact positions of the cysteines in the C-terminal arm of SUDV VP40. The cysteines and/or their redox status are critically involved in the differential regulation of viral budding and viral RNA synthesis.

PubMed: 37392738
DOI: 10.1016/j.str.2023.06.004

実験手法

X-RAY DIFFRACTION (1.7 Å)